ID   LSB3_YEAS7              Reviewed;         459 AA.
AC   A7A261;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 2.
DT   03-AUG-2022, entry version 49.
DE   RecName: Full=LAS seventeen-binding protein 3;
DE            Short=LAS17-binding protein 3;
GN   Name=LSB3; ORFNames=SCY_1771;
OS   Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=307796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJM789;
RX   PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA   Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA   Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA   Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA   Steinmetz L.M.;
RT   "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT   strain YJM789.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
CC   -!- SUBUNIT: Interacts with LAS17. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- PTM: Phosphorylation of Ser-397 is induced 2-fold in response to mating
CC       pheromone. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SH3YL1 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EDN59172.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AAFW02000176; EDN59172.1; ALT_SEQ; Genomic_DNA.
DR   AlphaFoldDB; A7A261; -.
DR   SMR; A7A261; -.
DR   PRIDE; A7A261; -.
DR   EnsemblFungi; EDN59172; EDN59172; SCY_1771.
DR   HOGENOM; CLU_015320_2_0_1; -.
DR   Proteomes; UP000007060; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   CDD; cd11525; SYLF_SH3YL1_like; 1.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR033643; SYLF_SH3YL1-like.
DR   InterPro; IPR007461; Ysc84_actin-binding.
DR   Pfam; PF00018; SH3_1; 1.
DR   Pfam; PF04366; Ysc84; 1.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF50044; SSF50044; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Phosphoprotein; SH3 domain.
FT   CHAIN           1..459
FT                   /note="LAS seventeen-binding protein 3"
FT                   /id="PRO_0000345086"
FT   DOMAIN          400..459
FT                   /note="SH3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   REGION          219..403
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        244..270
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        316..332
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        348..373
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        374..403
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         227
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P43603"
FT   MOD_RES         298
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P43603"
FT   MOD_RES         300
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P43603"
FT   MOD_RES         303
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P43603"
FT   MOD_RES         393
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P43603"
FT   MOD_RES         397
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P43603"
FT   MOD_RES         402
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P43603"
FT   MOD_RES         416
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P43603"
SQ   SEQUENCE   459 AA;  49344 MW;  F486C787B5771AAC CRC64;
     MGINNPIPRS LKSETKKAAK ILASFVKPNQ VFGADQVIPP DVLKRAKGLA IITILKAGFL
     FSGRAGSGVI VARLKDGTWS APSAIAMAGA GAGGMVGIEL TDFVFILNTQ DAVKSFSEFG
     TITLGGNVSV SAGPLGRSAE AAASASAGGV AAVFAYSKSK GLFAGVSVEG SAIIERREAN
     RKFYGDNCTA KMILSGRIRP PPAVDPLFRV LESRAFNYRP SNGGRGSFDD DEDDYYDDDD
     YYNDIPSSFS STDASSTRPN TRSTRRRAQS GSRYTFDDDD DDDDYGTGYS RNSRLAPTNS
     GGSGGKLDDP SGASSYYASH RRSGTAQSRA RSSRNRWADD EYDDYDDDYE SGYRRGNGRD
     RTKDREVDDL SNRFSKSRIS SASTPQTSQG RFTAPTSPST SSPKAVALYS FAGEESGDLP
     FRKGDVITIL KKSDSQNDWW TGRVNGREGI FPANYVELV